Espada Rocío, Parra R Gonzalo, Sippl Manfred J, Mora Thierry, Walczak Aleksandra M, Ferreiro Diego U
Protein Physiology Lab, Dep de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICEN, Buenos Aires, C1430EGA, Argentina.
Center of Applied Molecular Engineering, Division of Bioinformatics, Department of Molecular Biology, University of Salzburg, 5020 Salzburg, Austria.
Biochem Soc Trans. 2015 Oct;43(5):844-9. doi: 10.1042/BST20150083.
Structural domains are believed to be modules within proteins that can fold and function independently. Some proteins show tandem repetitions of apparent modular structure that do not fold independently, but rather co-operate in stabilizing structural forms that comprise several repeat-units. For many natural repeat-proteins, it has been shown that weak energetic links between repeats lead to the breakdown of co-operativity and the appearance of folding sub-domains within an apparently regular repeat array. The quasi-1D architecture of repeat-proteins is crucial in detailing how the local energetic balances can modulate the folding dynamics of these proteins, which can be related to the physiological behaviour of these ubiquitous biological systems.
结构域被认为是蛋白质中的模块，能够独立折叠并发挥功能。一些蛋白质呈现出明显模块化结构的串联重复，这些重复结构并非独立折叠，而是协同作用以稳定包含多个重复单元的结构形式。对于许多天然重复蛋白而言，研究表明重复单元之间的弱能量联系会导致协同性的破坏，并在看似规则的重复阵列中出现折叠亚结构域。重复蛋白的准一维结构对于详细阐述局部能量平衡如何调节这些蛋白质的折叠动力学至关重要，而这可能与这些普遍存在的生物系统的生理行为相关。
